ID A0A074YBR4_AURSE Unreviewed; 2085 AA.
AC A0A074YBR4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 28-JAN-2026, entry version 48.
DE RecName: Full=Fatty acid synthase subunit beta {ECO:0000256|ARBA:ARBA00068309};
DE EC=1.3.1.9 {ECO:0000256|ARBA:ARBA00012996};
DE EC=2.3.1.38 {ECO:0000256|ARBA:ARBA00013256};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.86 {ECO:0000256|ARBA:ARBA00012878};
DE EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
DE EC=4.2.1.59 {ECO:0000256|ARBA:ARBA00013167};
GN ORFNames=AUEXF2481DRAFT_6540 {ECO:0000313|EMBL:KEQ93464.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ93464.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ93464.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ93464.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit
CC contains domains for: [acyl-carrier-protein] acetyltransferase and
CC malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-
CC [acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-
CC protein] dehydratase. {ECO:0000256|ARBA:ARBA00058855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-
CC [ACP] + H(+); Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC Evidence={ECO:0000256|ARBA:ARBA00048536};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC Evidence={ECO:0000256|ARBA:ARBA00001055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC NADH + H(+); Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00048572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-
CC chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).; EC=2.3.1.86;
CC Evidence={ECO:0000256|ARBA:ARBA00048237};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446; EC=2.3.1.38;
CC Evidence={ECO:0000256|ARBA:ARBA00048835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00048462};
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000256|ARBA:ARBA00033756}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000256|ARBA:ARBA00010009, ECO:0000256|PIRNR:PIRNR005562}.
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DR EMBL; KL584765; KEQ93464.1; -; Genomic_DNA.
DR RefSeq; XP_013341941.1; XM_013486487.1.
DR FunCoup; A0A074YBR4; 600.
DR STRING; 1043005.A0A074YBR4; -.
DR GeneID; 25370084; -.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; A0A074YBR4; -.
DR OMA; HFMDNYG; -.
DR OrthoDB; 5417908at2759; -.
DR Proteomes; UP000030641; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03447; FAS_MaoC; 1.
DR FunFam; 1.20.1050.120:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 1.20.930.70:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.10.129.10:FF:000017; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.20.20.70:FF:000078; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.30.1120.100:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.10.129.10:FF:000015; Fatty acid synthase subunit beta; 1.
DR FunFam; 3.20.20.70:FF:000169; Fatty acid synthase subunit beta; 1.
DR FunFam; 3.30.70.3330:FF:000001; Fatty acid synthase subunit beta dehydratase; 1.
DR FunFam; 3.40.366.10:FF:000003; Fatty acid synthase subunit beta dehydratase; 1.
DR Gene3D; 1.20.1050.120; -; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.1120.100; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR039569; FAS1-like_DH_region.
DR InterPro; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR041099; FAS1_N.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR050830; Fungal_FAS.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF13452; FAS1_DH_region; 1.
DR Pfam; PF22235; FAS1_thioest_ins; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR005562};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR005562};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR005562};
KW Reference proteome {ECO:0000313|Proteomes:UP000030641};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1689..2010
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 282
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1833
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2085 AA; 230393 MW; 79ED12F3FE65BA10 CRC64;
MYGSGSQTGV STPRSQAVSR PLILSHGSLE YSFLIPTALH FSASQLKDAF IATLPTPTDE
LAQDDEPSSV TELVARYIGF VARECDEGDD PGSFEEVLKL VLHEFERAFL RGNEVHAIAA
SLPGIYEKKL ATVSSYYAAR AAVSRPIKSH ESALLREAAD ENAFIYAVFG GQGNIEEYFE
ELREIYTTYP SFVEDFITAA AAHLQTLSRE PQVEKLYPKG LDVMRWLHNK DAQPDIDYLV
SAPVSLPLIG LTQLAHFVVT CRVLGTHPGN VRDRLSGTTG HSQGVVTAAA IAASKSWETF
DKASRDALSI LFWIGSRSQQ AYPRTSLAPS TLQDSIDSGE GTPTPMLSIR DLTREAVQTH
IDATNQHLPE DRHIAISLVN SARNFVVTGP PMSLYGLNLR LRKVKAPTGL DQSRIPFTDR
KVRFVNRFLP ITAPFHSKYL AEADAHLQED LKDIVIPSSD LGIPLFDTNT GKDISQESAD
NIVPHLVRMI TQDSVNWETA TVFPRATHVL DFGPGGISGL GVLTNRNKDG TGVRVILAGT
MDGTNVEVGY KPEIFDRDAE HAVKYAVDWV KEHGPKLART SAGQTFVDTK MSRMLGLPPV
MVAGMTPCTV VTDFVSATMN AGYEIELAGG GYFTDAKMTE AIAKIEKSIP AGRGISINLI
YVSPQAMAWQ IPMIARLRAD GVPIESLTIG AGVPSIEVAN EYIQTLGIKR IAFKPGSVEA
IQSCINIAKA NPGFPVIMQW TGGRGGGHHS FEDFHQPMFQ MYGRIRKCPN LVLIAGSGFG
AAEDTYPYLT GQWASKFGYP PMPFDGVLFG SRVMVAKEAK TAPAAKQAIV DAPGLDDADW
EKTYKGEAGG VITVRSEMGE PIHKLATRGV KFWAEMDQKI FSLDKAKRIP ELKKNRDHII
KKLNDDFQKV WFGRNSAGVS VDLEDMTYAE VVHRMVELMY VKKEKRWIDP SLARLTVDFI
RRVEERFTTA ANKSSLVQNY AEMNEPFAVV EKFVAAYPEA DKQLINAQDV QHFIQLCQRR
GQKPVPFVPA LDGSFEFFFK KDSLWQSEDL AAVVGEDVGR TCILQGPMAV KYSTKVDEPI
KEILDGVHEG HIQYLLRDFY GGDESKIPVV EYFGGKLVEA SDEIDVEGLT VSELNNKTIY
RLSASPSAAL PKSDSWLSLL AGKTYSWRHA FFTADVFVQG QRFNTNPMQR IFAPAPGMMV
EINYPNDPSK TVITVKEPTS SGKFVQTIEI GPIANNEITV KLIEERSATH SPVALPLKFT
YHPETGYAPI REVMDARNDR IKEFYYKIWF GDADVPFDTP VTSRFDGGRA TVTSEAINDF
VHAVGNTGEA FVDRPGKEVF APMDFAIVVG WKAITKPIFP RKIDGDLLKL VHLSNGFRMI
PGAAPLKKGD VLDTTAEVNA VINQASGKMV EVCGTITRDG KPVMEVTSQF LYRGAYTDFE
NTFQRKTEKP MQITLATSKD VAVLQSKEWF RLEDTEIDLL GQTITFRLQS LVRYKNENVF
STVETVGQVE IELPSKEIIQ LASVEYEAGV SHGNPVIDYL ERHGSAIDQP VNFENPIPLN
GKTPLELKAP ASNETYAKVS GDYNPIHVSR VFSKYANLPG TITHGMYSSA AVRSLVETWA
AENNVGRVRS FHVNLVGMVL PNDTIQVTLQ HIGMVSGRKI ITVEARNKET EDKVLIGEAE
VEQPVSAYVF TGQGSQEQGM GMELYASSPV AKEVWDRADK HFLDNYGFAI TNIVKNNPNE
MTVHFGGPRG KAIRQNYMSM TFETVAADGS IKSEKIFKEV NESTTSYTYR SPTGLLSATQ
FTQPALTLME KASFEDMRSK GLVQRDSTFA GHSLGEYSAL AAMAEVMPIE SLVSVVFYRG
LTMQVAVERD EAGRSNYSMC AVNPSRIGKT FTEQALQYVV ENIAETTTWL LEIVNYNIAN
MQYVAAGDLR ALDCLANVLN YLKVQKIDIQ SLMQTMSLED VKSHLVEIIK GCAEQTEAKP
KPLDLQRGFA TIPLKGIDVP FHSTFLRSGV KPFRSFLLKK INKTSIDPSK LVGKYIPNVT
ARPFEITKEY FEDVYRLTNS PKIGNILANW ESYVNDDGSK PAPAA
//
